3S43
HIV-1 protease triple mutants V32I, I47V, V82I with antiviral drug amprenavir
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-03-18 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.8 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.374, 86.565, 46.306 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.260 |
| R-factor | 0.1602 |
| Rwork | 0.160 |
| R-free | 0.20020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3djk |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.031 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.310 |
| High resolution limit [Å] | 1.260 | 1.260 |
| Rmerge | 0.063 | 0.361 |
| Number of reflections | 58771 | |
| <I/σ(I)> | 14.5 | 2.1 |
| Completeness [%] | 91.3 | 59.9 |
| Redundancy | 3.7 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.4 | 298 | FROM A 3.5MG/ML PROTEIN SOLUTION AT PH 5.4 WITH 0.175M KI, 0.1M CITRATE PHOSPHATE, 4% DMSO. 1.0ul WELL SOLUTION WITH 1.5ul PROTEIN SOLUTION. THE INHIBITOR WAS MIXED WITH PROTEASE IN A RATIO 5:1, EVAPORATION, TEMPERATURE 298K, VAPOR DIFFUSION, HANGING DROP |
